AUF1 and HuR proteins stabilize interleukin-8 mRNA in human saliva.
AUF1 and HuR proteins stabilize interleukin-8 mRNA in human saliva.
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DOI：
10.1177/154405910808700803
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发表时间：
2008-08
影响因子：
7.6
通讯作者：
Wong DT
中科院分区：
文献类型：
--
作者：
Palanisamy V;Park NJ;Wang J;Wong DT
人类唾液含有数千种mRNA，其中一些具有翻译价值，可作为人类疾病的诊断标志物。我们发现在人类唾液中检测到的mRNA中有超过30%的mRNA在其3′非翻译区（3′UTR）含有富含AU的元件（ARE）。由于战神已知通过与ARE结合蛋白形成复合物来促进RNA周转，因此我们假设唾液mRNA的稳定性是由人唾液中的ARE结合蛋白介导的。为了验证这一假设，我们监测了放射性标记的ARE-唾液蛋白提取物中的唾液mRNA（IL-8）的体外降解。通过加入过量的含有4个串联战神的未标记IL-8 mRNA片段，竞争唾液ARE结合蛋白，加速IL-8 mRNA的降解。UV交联和免疫沉淀实验显示，2 ARE结合蛋白，AUF 1和HuR，与IL-8 mRNA在唾液中。这些结果表明ARE结合蛋白有助于ARE mRNA在人唾液中的稳定性。
Human saliva contains thousands of mRNAs, some of which have translational value as diagnostic markers for human diseases. We have found that more than 30% of the mRNAs detected in human saliva contain AU-rich elements (ARE) in their 3′ untranslated regions (3′UTR). Since AREs are known to contribute to RNA turnover by forming complexes with ARE-binding proteins, we hypothesized that salivary mRNA stability is mediated by ARE-binding proteins in human saliva. To test this hypothesis, we monitored the in vitro degradation of a radiolabeled ARE-containing salivary mRNA (IL-8) in salivary protein extracts. The degradation of IL-8 mRNA was accelerated by competition for saliva ARE-binding proteins through the addition of excess unlabeled IL-8 mRNA fragments containing 4 tandem AREs. UV cross-linking and immunoprecipitation experiments revealed 2 ARE-binding proteins, AUF1 and HuR, associated with IL-8 mRNA in saliva. These results demonstrate that ARE-binding proteins contribute to the stability of ARE mRNAs in human saliva.
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